Interactions of monoamine oxidases with the antiepileptic drug zonisamide: specificity of inhibition and structure of the human monoamine oxidase b complex.
The binding of zonisamide to purified, recombinant monoamine oxidases (MAOs) has
been investigated. It is a competitive inhibitor of human MAO B (K(i) = 3.1 ±
0.3 μM), of rat MAO B (K(i) = 2.9 ± 0.5 μM), and of zebrafish MAO (K(i) =
30.8 ± 5.3 μM). No inhibition is observed with purified human or rat MAO A.
The 1.8 Å structure of the MAO B complex demonstrates that it binds within the
substrate cavity.